Locally Resolved Membrane Binding Affinity of the N-Terminus of α-Synuclein

M. Robotta, C. Hintze, S. Schildknecht, Niels Zijlstra, C. Jungst, C. Karreman, M. Huber, M. Leist, Vinod Subramaniam, M. Drescher

Research output: Contribution to journalArticleAcademicpeer-review

23 Citations (Scopus)

Abstract

α-Synuclein is abundantly present in Lewy bodies, characteristic of Parkinson’s disease. Its exact physiological role has yet to be determined, but mitochondrial membrane binding is suspected to be a key aspect of its function. Electron paramagnetic resonance spectroscopy in combination with site-directed spin labeling allowed for a locally resolved analysis of the protein–membrane binding affinity for artificial phospholipid membranes, supported by a study of binding to isolated mitochondria. The data reveal that the binding affinity of the N-terminus is nonuniform
Original languageUndefined
Pages (from-to)3960-3962
Number of pages3
JournalBiochemistry (USA)
Volume51
Issue number19
DOIs
Publication statusPublished - 2012

Keywords

  • METIS-289434
  • IR-84730

Cite this